Source:http://linkedlifedata.com/resource/pubmed/id/10488134
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
39
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pubmed:dateCreated |
1999-11-4
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pubmed:abstractText |
The HB-19 pseudopeptide 5[Kpsi(CH(2)N)PR]-TASP, psi(CH(2)N) for reduced peptide bond, is a specific inhibitor of human immunodeficiency virus (HIV) infection in different CD4(+) cell lines and in primary T-lymphocytes and macrophages. Here, by using an experimental CD4(+) cell model to monitor HIV entry and infection, we demonstrate that HB-19 binds the cell surface and inhibits attachment of HIV particles to permissive cells. At concentrations that inhibit HIV attachment, HB-19 binds cells irreversibly, becomes complexed with the cell-surface-expressed nucleolin, and eventually results in its degradation. Accordingly, by confocal immunofluorescence microscopy, we demonstrate the drastic reduction of the cell-surface-expressed nucleolin following treatment of cells with HB-19. HIV particles can prevent the binding of HB-19 to cells and inhibit complex formation with nucleolin. Such a competition between viral particles and HB-19 is consistent with the implication of nucleolin in the process of HIV attachment to target cells. We show that another inhibitor of HIV infection, the fibroblast growth factor-2 (FGF-2) that uses cell-surface-expressed heparan sulfate proteoglycans as low affinity receptors, binds cells and blocks attachment of HIV to permissive cells. FGF-2 does not prevent the binding of HB-19 to cells and to nucleolin, and similarly HB-19 has no apparent effect on the binding of FGF-2 to the cell surface. The lack of competition between these two anti-HIV agents rules out the potential involvement of heparan sulfate proteoglycans in the mechanism of anti-HIV effect of HB-19, thus pointing out that nucleolin is its main target.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-HIV Agents,
http://linkedlifedata.com/resource/pubmed/chemical/CP 51,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Heparan Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Ethers,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nucleolin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27875-84
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10488134-Anti-HIV Agents,
pubmed-meshheading:10488134-Binding Sites,
pubmed-meshheading:10488134-CD4-Positive T-Lymphocytes,
pubmed-meshheading:10488134-Cell Line,
pubmed-meshheading:10488134-Cell Membrane,
pubmed-meshheading:10488134-Fibroblast Growth Factor 2,
pubmed-meshheading:10488134-Flow Cytometry,
pubmed-meshheading:10488134-HIV-1,
pubmed-meshheading:10488134-Heparan Sulfate Proteoglycans,
pubmed-meshheading:10488134-Humans,
pubmed-meshheading:10488134-Microscopy, Confocal,
pubmed-meshheading:10488134-Oligopeptides,
pubmed-meshheading:10488134-Peptides,
pubmed-meshheading:10488134-Phospholipid Ethers,
pubmed-meshheading:10488134-Phosphoproteins,
pubmed-meshheading:10488134-Proteins,
pubmed-meshheading:10488134-RNA-Binding Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans.
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pubmed:affiliation |
Unité de Virologie et Immunologie Cellulaire, URA 1930 CNRS, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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